2b2r
From Proteopedia
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Crystal structure of an oxoferryl species of catalase-peroxidase KATG at pH5.6
Overview
The catalase reaction of catalase-peroxidases involves catalase-specific features built into a peroxidase core. An arginine, 20 A from the active-site heme, acts as a molecular switch moving between two conformations, one that activates heme oxidation and one that activates oxoferryl heme reduction by H(2)O(2), facilitating the catalatic pathway in a peroxidase. The influence of the arginine is imparted to the heme through its association with or dissociation from a tyrosinate that modulates reactivity through a Met-Tyr-Trp crosslinked adduct and a pi electron interaction of the heme with the adduct Trp.
About this Structure
2B2R is a Single protein structure of sequence from Burkholderia pseudomallei with , and as ligands. Active as Catalase, with EC number 1.11.1.6 Full crystallographic information is available from OCA.
Reference
A molecular switch and electronic circuit modulate catalase activity in catalase-peroxidases., Carpena X, Wiseman B, Deemagarn T, Singh R, Switala J, Ivancich A, Fita I, Loewen PC, EMBO Rep. 2005 Dec;6(12):1156-62. PMID:16211084
Page seeded by OCA on Thu Feb 21 16:33:31 2008
Categories: Burkholderia pseudomallei | Catalase | Single protein | Carpena, X. | Deemagarn, T. | Fita, I. | Ivancich, A. | Loewen, P C. | Singh, R. | Switala, J. | Wiseman, B. | HEM | NA | O | Catalase-peroxidase | Compound i | Katg | Oxoferryl species
